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Cell and Organelle Structure and Assembly

Mitochondrial Import Driving Forces: Enhanced Trapping by Matrix Hsp70 Stimulates Translocation and Reduces the Membrane Potential Dependence of Loosely Folded Preproteins

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Pages 7097-7104 | Received 09 Mar 2001, Accepted 19 Jul 2001, Published online: 27 Mar 2023

REFERENCES

  • Alconada, A., F. Gärtner, A. Hönlinger, M. Kübrich, and N. Pfanner. 1995. Mitochondrial receptor complex from Neurospora crassa and Saccharomyces cerevisiae. Methods Enzymol. 260:263–286.
  • Bauer, M. F., S. Hofmann, W. Neupert, and M. Brunner. 2000. Protein translocation into mitochondria: the role of TIM complexes. Trends Cell Biol. 10:25–31.
  • Bauer, M. F., C. Sirrenberg, W. Neupert, and M. Brunner. 1996. Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria. Cell 87:33–41.
  • Bömer, U., A. Maarse, F. Martin, A. Geissler, A. Merlin, B. Schonfisch, M. Meijer, N. Pfanner, and J. Rassow. 1998. Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins. EMBO J. 17:4226–4237.
  • Bukau, B., and A. Horwich. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92:351–366.
  • Cyr, D. M., R. Stuart, and W. Neupert. 1993. A matrix ATP requirement for presequence translocation across the inner membrane of mitochondria. J. Biol. Chem. 268:23751–23754.
  • Ellis, R. J., and S. van der Vies. 1991. Molecular chaperones. Annu. Rev. Biochem. 60:321–347.
  • Gambill, B. D., W. Voos, P. Kang, B. Miao, T. Langer, E. Craig, and N. Pfanner. 1993. A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins. J. Cell Biol. 123:109–117.
  • Gärtner, F., W. Voos, E. Craig, M. Cumsky, and N. Pfanner. 1995. Mitochondrial import of subunit Va of cytochrome c oxidase characterized with yeast mutants. Independence from receptors, but requirement for matrix hsp70 translocase function. J. Biol. Chem. 270:3788–3795.
  • Gaume, B., C. Klaus, C. Ungermann, B. Guiard, and M. Brunner. 1998. Unfolding of preproteins upon import into mitochondria. EMBO J. 17:6497–6507.
  • Geissler, A., T. Krimmer, U. Bömer, B. Guiard, J. Rassow, and N. Pfanner. 2000. Membrane potential-driven protein import into mitochondria: the sorting sequence of cytochrome b2 modulates the Δψ-dependence of translocation of the matrix-targeting sequence. Mol. Biol. Cell 11:3977–3991.
  • Geissler, A., T. Krimmer, B. Schönfisch, M. Meijer, and J. Rassow. 2000. Biogenesis of the yeast frataxin homolog Yfh1p: Tim44-dependent transfer to mtHsp70 facilitates folding of newly imported proteins in mitochondria. Eur. J. Biochem. 267:3167–3180.
  • Glick, B. S.. 1995. Can Hsp70 proteins act as force-generating motors?. Cell 80:11–14.
  • Glick, B. S., C. Wachter, G. Reid, and G. Schatz. 1993. Import of cytochrome b2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP. Protein Sci. 2:1901–1917.
  • Hartl, F. U.. 1996. Molecular chaperones in cellular protein folding. Nature 381:571–579.
  • Haucke, V., and G. Schatz. 1997. Reconstitution of the protein insertion machinery of the mitochondrial inner membrane. EMBO J. 16:4560–4567.
  • Horst, M., W. Oppliger, B. Feifel, G. Schatz, and B. S. Glick. 1996. The mitochondrial protein import motor: dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis. Protein Sci. 5:759–767.
  • Huang, S., K. Ratliff, M. Schwartz, J. Spenner, and A. Matouschek. 1999. Mitochondria unfold precursor proteins by unraveling them from their N-termini. Nat. Struct. Biol. 6:1132–1138.
  • Jensen, R. E., and A. Johnson. 1999. Protein translocation: is Hsp70 pulling my chain?. Curr. Biol. 9:R779–R782.
  • Kang, P. J., J. Ostermann, J. Shilling, W. Neupert, E. Craig, and N. Pfanner. 1990. Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature 348:137–143.
  • Kronidou, N. G., W. Oppliger, L. Bolliger, K. Hannavy, B. Glick, G. Schatz, and M. Horst. 1994. Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane. Proc. Natl. Acad. Sci. USA 91:12818–12822.
  • Lim, J. H., F. Martin, B. Guiard, N. Pfanner, and W. Voos. 2001. The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation. EMBO J. 20:941–950.
  • Liu, Q., J. Krzewska, K. Liberek, and E. Craig. 2001. Mitochondrial Hsp70 Ssc1: role in protein folding. J. Biol. Chem. 276:6112–6118.
  • Martin, J., K. Mahlke, and N. Pfanner. 1991. Role of an energized inner membrane in mitochondrial protein import: Δψ drives the movement of presequences. J. Biol. Chem. 266:18051–18057.
  • Matlack, K. E., B. Misselwitz, K. Plath, and T. A. Rapoport. 1999. BiP acts as a molecular ratchet during posttranslational transport of prepro-α factor across the ER membrane. Cell 97:553–564.
  • Matouschek, A., A. Azem, K. Ratliff, K. Schmid, and G. Schatz. 1997. Active unfolding of precursor proteins during mitochondrial protein import. EMBO J. 16:6727–6736.
  • Moro, F., C. Sirrenberg, H. Schneider, W. Neupert, and M. Brunner. 1999. The TIM17 · 23 preprotein translocase of mitochondria: composition and function in protein transport into the matrix. EMBO J. 18:3667–3675.
  • Neupert, W.. 1997. Protein import into mitochondria. Annu. Rev. Biochem. 66:863–917.
  • Paunola, E., T. Suntio, E. Jamsa, and M. Makarow. 1998. Folding of active β-lactamase in the yeast cytoplasm before translocation into the endoplasmic reticulum. Mol. Biol. Cell 9:817–827.
  • Pfanner, N., E. Craig, and A. Hönlinger. 1997. Mitochondrial preprotein translocase. Annu. Rev. Cell Dev. Biol. 13:25–51.
  • Pfanner, N., and M. Meijer. 1995. Protein sorting: pulling in the proteins. Curr. Biol. 5:132–135.
  • Pfanner, N., and W. Neupert. 1985. Transport of proteins into mitochondria: a potassium diffusion potential is able to drive the import of ADP/ATP carrier. EMBO J. 4:2819–2825.
  • Pilon, M., and R. Schekman. 1999. Protein translocation: how Hsp70 pulls it off. Cell 97:679–682.
  • Rassow, J., A. Maarse, E. Krainer, M. Kübrich, M. Meijer, E. Craig, and N. Pfanner. 1994. Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44. J. Cell Biol. 127:1547–1556.
  • Schatz, G., and B. Dobberstein. 1996. Common principles of protein translocation across membranes. Science 271:1519–1526.
  • Scherer, P. E., U. Krieg, S. Hwang, D. Vestweber, and G. Schatz. 1990. A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein. EMBO J. 9:4315–4322.
  • Schleyer, M., and W. Neupert. 1985. Transport of proteins into mitochondria: translocational intermediates spanning contact sites between outer and inner membranes. Cell 43:339–350.
  • Schneider, H. C., J. Berthold, K. Dietmeier, B. Guiard, M. Brunner, and W. Neupert. 1994. Mitochondrial Hsp70/MIM44 complex facilitates protein import. Nature 371:768–774.
  • Schneider, H. C., B. Westermann, W. Neupert, and M. Brunner. 1996. The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import. EMBO J. 15:5796–5803.
  • Söllner, T., J. Rassow, and N. Pfanner. 1991. Analysis of mitochondrial protein import using translocation intermediates and specific antibodies. Methods Cell Biol. 34:345–358.
  • Ungermann, C., B. Guiard, W. Neupert, and D. Cyr. 1996. The Δψ- and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria. EMBO J. 15:735–744.
  • Ungermann, C., W. Neupert, and D. Cyr. 1994. The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria. Science 266:1250–1253.
  • Vogel, J. P., L. Misra, and M. Rose. 1990. Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast. J. Cell Biol. 110:1885–1895.
  • Voisine, C., E. Craig, N. Zufall, O. von Ahsen, N. Pfanner, and W. Voos. 1999. The protein import motor of mitochondria: unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70. Cell 97:565–574.
  • von Ahsen, O., W. Voos, H. Henninger, and N. Pfanner. 1995. The mitochondrial protein import machinery: role of ATP in dissociation of the Hsp70 · Mim44 complex. J. Biol. Chem. 270:29848–29853.
  • Voos, W., B. Gambill, S. Laloraya, D. Ang, E. Craig, and N. Pfanner. 1994. Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes. Mol. Cell. Biol. 14:627–663.
  • Voos, W., B. Gambill, B. Guiard, N. Pfanner, and E. Craig. 1993. Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix. J. Cell Biol. 123:119–126.
  • Voos, W., O. von Ahsen, H. Müller, B. Guiard, J. Rassow, and N. Pfanner. 1996. Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins. EMBO J. 15:2668–2677.
  • Walter, P., and A. Johnson. 1994. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10:87–119.

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